Bioprocess and Biosystems Engineering

, Volume 41, Issue 6, pp 793–802 | Cite as

Different strategies for multi-enzyme cascade reaction for chiral vic-1,2-diol production

  • Ana Vrsalović Presečki
  • Lela Pintarić
  • Anera Švarc
  • Đurđa Vasić-Rački
Research Paper
  • 109 Downloads

Abstract

The stereoselective three-enzyme cascade for the one-pot synthesis of (1S,2S)-1-phenylpropane-1,2-diol ((1S,2S)-1-PPD) from inexpensive starting substrates, benzaldehyde and acetaldehyde, was explored. By coupling stereoselective carboligation catalyzed by benzoylformate decarboxylase (BFD), L-selective reduction of a carbonyl group with alcohol dehydrogenase from Lactobacillus brevis (ADHLb) as well as the coenzyme regeneration by formate dehydrogenase (FDH), enantiomerically pure diastereoselective 1,2-diol was produced. Two different multi-enzyme system approaches were applied: the sequential two-step one-pot and the simultaneous one-pot cascade. All enzymes were kinetically characterized. The impact of acetaldehyde on the BFD and ADHLb stability was investigated. To overcome the kinetic limitation of acetaldehyde in the carboligation reaction and to reduce its influence on the enzyme stability, experiments were performed in two different excesses of acetaldehyde (100 and 300%). Due to the ADHLb deactivation by acetaldehyde, the simultaneous one-pot cascade proved not to be the first choice for the investigated three-enzyme system. In the sequential cascade with 300% acetaldehyde excess a 100% yield of vic 1,2-diol was reached.

Keywords

Multi-enzyme cascade reaction Asymmetric reduction Stereoselectivity Alcohol dehydrogenase Benzoylformate decarboxylase 

Notes

Acknowledgements

This work was supported by University of Zagreb short-term financial scientific research support under the title “Mathematical modeling of the biocatalytic synthesis of industrially interesting products”. The authors would like to thank Prof. Martina Pohl from the Institute of Bio- and Geosciences, IBG-1: Biotechnology, Research center Jülich, Germany for the gift of alcohol dehydrogenase from Lactobacillus brevis and Davor Valinger from Faculty of Food Technology and Biotechnology, University of Zagreb for the isolation of enzyme benzoylformate decarboxylase.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

449_2018_1912_MOESM1_ESM.docx (198 kb)
Supplementary material 1 (DOCX 197 KB)

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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  • Ana Vrsalović Presečki
    • 1
  • Lela Pintarić
    • 2
  • Anera Švarc
    • 1
  • Đurđa Vasić-Rački
    • 1
  1. 1.Faculty of Chemical Engineering and TechnologyUniversity of ZagrebZagrebCroatia
  2. 2.Faculty of Textile TechnologyUniversity of ZagrebZagrebCroatia

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